Molecular cloning and expression of cDNA for mammalian translation initiation factor 5. | Zendy

Kanak Das Dhruba Das | Zendy; J Chevesich | Zendy; Umadas Maitra | Zendy

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Molecular cloning and expression of cDNA for mammalian translation initiation factor 5.

Author(s) -

Kanak Das Dhruba Das,

J Chevesich,

Umadas Maitra

Publication year - 1993

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.90.7.3058

Subject(s) - eukaryotic initiation factor , initiation factor , complementary dna , eif4a1 , biology , gtpase , ribosomal protein , eukaryotic small ribosomal subunit , eif2 , microbiology and biotechnology , eukaryotic translation , eukaryotic translation initiation factor 4 gamma , peptide sequence , eukaryotic ribosome , biochemistry , translation (biology) , ribosome , messenger rna , gene , rna

Eukaryotic translation initiation factor 5 (eIF-5) catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.AUG.Met-tRNAf-eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the formation of a functional 80S initiation complex. A rat cDNA that encodes eIF-5 has been isolated and expressed in Escherichia coli to yield a catalytically active eIF-5 protein. The 3.55-kb cDNA encodes a protein of 429 amino acids (calculated M(r) 48,926) with properties that are similar to eIF-5 isolated from rabbit reticulocyte lysates. The deduced amino acid sequence of eIF-5 contains sequence motifs characteristic of proteins of the GTPase superfamily.

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